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Title of Journal: Protein J

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Abbravation: The Protein Journal

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Springer US

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10.1007/978-3-319-51292-1_6

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1573-4943

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The Role of Strong Electrostatic Interactions at t

Authors: Margarita C De Jesus Brandall L Ingle Khaldoon A Barakat Bisesh Shrestha Kerri D Slavens Thomas R Cundari Mary E Anderson
Publish Date: 2014/07/29
Volume: 33, Issue: 5, Pages: 403-409
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Abstract

The obligate homodimer human glutathione synthetase hGS provides an ideal system for exploring the role of protein–protein interactions in the structural stability activity and allostery of enzymes The two active sites of hGS which are 40 Å apart display allosteric modulation by the substrate γglutamylcysteine γGC during the synthesis of glutathione a key cellular antioxidant The two subunits interact at a relatively small dimer interface dominated by electrostatic interactions between S42 R221 and D24 Alanine scans of these sites result in enzymes with decreased activity altered γGC affinity and decreased thermal stability Molecular dynamics simulations indicate these mutations disrupt interchain bonding and impact the tertiary structure of hGS While the ionic hydrogen bonds and salt bridges between S42 R221 and D24 do not mediate allosteric communication in hGS these interactions have a dramatic impact on the activity and structural stability of the enzyme

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